The Lysozyme from Insect (Manduca sexta) Is a Cold-Adapted Enzyme
Authors: Rogerio R. Sotelo-Mundo; Alonso A. Lopez-Zavala; Karina D. Garcia-Orozco; Aldo A. Arvizu-Flores; Enrique F. Velazquez-Contreras; Elisa M. Valenzuela-Soto; Arturo Rojo-Dominguez; Michael R. Kanost
Source: Protein and Peptide Letters, Volume 14, Number 8, August 2007 , pp. 774-778(5)
Publisher: Bentham Science Publishers
Abstract:Enzymatic activity is dependent on temperature, although some proteins have evolved to retain activity at low temperatures at the expense of stability. Cold adapted enzymes are present in a variety of organisms and there is ample interest in their structure-function relationships. Lysozyme (E.C. 220.127.116.11) is one of the most studied enzymes due to its antibacterial activity against Gram positive bacteria and is also a cold adapted protein. In this work the characterization of lysozyme from the insect Manduca sexta and its activity at low temperatures is presented. Both M. sexta lysozymes natural and recombinant showed a higher content of α-helix secondary structure compared to that of hen egg white lysozyme and a higher specific enzymatic activity in the range of 5-30 °C. These results together with measured thermodynamic activation parameters support the designation of M. sexta lysozyme as a cold adapted enzyme. Therefore, the insect recombinant lysozyme is feasible as a model for structure-function studies for cold-adapted proteins.
Document Type: Research Article
Publication date: 2007-08-01
- Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.